Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins (Q24653757)

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English	Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins	scientific article

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Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins (English)

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Travis P Schrank

1

object named as

Travis P Schrank

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author name string

D Wayne Bolen

2

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Vincent J Hilser

3

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language of work or name

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publication date

6 October 2009

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Proceedings of the National Academy of Sciences of the United States of America

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106

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40

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16984-9

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Conformational transitions of adenylate kinase: switching by cracking

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

7 April 2017

Kemp elimination catalysts by computational enzyme design

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

7 April 2017

Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

7 April 2017

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

7 April 2017

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

7 April 2017

Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

7 April 2017

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

7 April 2017

Noncooperative folding of subdomains in adenylate kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Illuminating the mechanistic roles of enzyme conformational dynamics

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Conformational entropy in molecular recognition by proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Dynamically driven protein allostery.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Roles of static and dynamic domains in stability and catalysis of adenylate kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Psychrophilic enzymes: hot topics in cold adaptation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

28 September 2017

Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

30 May 2018

Validity of the "two-state" hypothesis for conformational transitions of proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

30 May 2018

Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

30 May 2018

Domain closure in adenylate kinase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2761315

30 May 2018

Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

1 reference

https://api.crossref.org/works/10.1073/PNAS.0906510106

21 January 2018

NMR identification of transient complexes critical to adenylate kinase catalysis

1 reference

https://api.crossref.org/works/10.1073/PNAS.0906510106

21 January 2018

Backbone Dynamics ofEscherichia coliAdenylate Kinase at the Extreme Stages of the Catalytic Cycle Studied by15N NMR Relaxation†

1 reference

https://api.crossref.org/works/10.1073/PNAS.0906510106

21 January 2018

Source of Catalysis in the Lactate Dehydrogenase System. Ground-State Interactions in the Enzyme.cntdot.Substrate Complex

1 reference

https://api.crossref.org/works/10.1073/PNAS.0906510106

21 January 2018

Allostery without conformational change. A plausible model

1 reference

https://pubmed.ncbi.nlm.nih.gov/19805185

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The magnitude of the backbone conformational entropy change in protein folding

1 reference

https://pubmed.ncbi.nlm.nih.gov/19805185

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Multinuclear magnetic resonance studies of Escherichia coli adenylate kinase in free and bound forms. Resonance assignment, secondary structure and ligand binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/19805185

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions

1 reference

https://pubmed.ncbi.nlm.nih.gov/19805185

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.0906510106

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2009PNAS..10616984S

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release_i2hp6wykhndg3hjjv2yhpp4j3i

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https://api.fatcat.wiki/v0/release/i2hp6wykhndg3hjjv2yhpp4j3i

24 November 2022

based on heuristic

mapped directly with Wikidata item

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PMC publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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